DELINEATION OF ANTIGEN CONTACT RESIDUES ON AN MHC CLASS-II MOLECULE

被引：66

作者：

PECCOUD, J

DELLABONA, P

ALLEN, P

BENOIST, C

MATHIS, D

机构：

[1] FAC MED STRASBOURG,INST CHIM BIOL,CNRS,GENET MOLEC EUCARYOTES LAB,INSERM,UA 184,F-67085 STRASBOURG,FRANCE

[2] WASHINGTON UNIV,SCH MED,DEPT PATHOL,ST LOUIS,MO 63110

来源：

EMBO JOURNAL | 1990年 / 9卷 / 13期

关键词：

ANTIGEN PRESENTATION; MAJOR HISTOCOMPATIBILITY COMPLEX; SITE-SPECIFIC MUTAGENESIS; T-CELL RECOGNITION;

D O I：

10.1002/j.1460-2075.1990.tb07869.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

This report describes a detailed mutational analysis of a major histocompatibility complex class II molecule-the alpha-chain of the A(k) complex. Each residue from 50-79 was replaced by an alanine, and the effects on recognition of A(k) by panels of antibodies and T cells determined. The results provide the strongest existing experimental evidence that the antigen binding site on a class II molecule can be modelled on the crystal structure of a class I molecule. The data have also permitted the delineation of residues that actually contact antigenic peptides.

引用

页码：4215 / 4223

页数：9

共 62 条

[1] EVIDENCE THAT MULTIPLE RESIDUES ON BOTH THE ALPHA-HELICES OF THE CLASS-I MHC MOLECULE ARE SIMULTANEOUSLY RECOGNIZED BY THE T-CELL RECEPTOR [J].